In vitro digestion of protein-enriched restructured beef steaks with pea protein isolate, rice protein and lentil flour following sous vide processing

Abstract

The effect of plant protein inclusion in cooked meat upon in vitro gastro-intestinal (GI) digestion was investigated. Pea protein isolate, rice protein and lentil flour were used to increase the protein content in a meat model system restructured using two transglutaminase enzymes [Activa®EB (TG) and Transgluseen™-M (TS)]. Restructured beef steaks were subjected to simulated GI digestion using the static INFOGEST method. Samples taken at different digestion times were analysed using SDS-PAGE, size exclusion-HPLC, free amino acid analysis and microscopy. SDS-PAGE analysis revealed significant protein hydrolysis during GI digestion. Most soluble peptides had a molecular weight smaller than 500 Da, corresponding to peptides of < 5 amino acids, regardless of food treatment. The amounts of released, free amino acids isoleucine, lysine, phenylalanine and valine were higher (P < 0.05) in lentil-enriched restructured beef steaks following GI digestion. Confocal laser scanning microscopy (CSLM) revealed pronounced aggregation in digested samples. In vitro digestates of protein-enriched restructured beef steaks showed lower production of small molecular weight peptides. This study demonstrated how the bioaccessibility of protein-enriched restructured beef steaks are influenced by formulation and processing.

Determination of the iron bioavailability, conformation, and rheology of iron‐binding proteins from Tegillarca granosa

“…TF, however, appeared to be more degradation‐resistant than BF (Figures 5 and 6) since a TF‐derived band was observed after 120 min digestion with trypsin. This suggests that TF could prolong gastric distension and satiation signals (Baugreet et al., 2019). These results also were shown in Figure 7 and Table 3, TH had the higher protein digestibility and degree of hydrolysis than BH under in vitro digestion, and the small peptide of digested solution in TH was more than BH, which meant TH was more easily digested to smaller peptide.…”

Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages.

“…In cooked restructured steaks the inclusion of pea protein isolate (8%) besides enhancing the protein content, increased hardness, chewiness, cohesiveness and gumminess due pea proteins ability to water and fat binding as well as gelling properties; and better when combined with transglutaminase uniform structure (Baugreet, Kerry, Allen, Gallagher, & Hamill, 2018), and high protein in vitro digestibility (high free amino acids isoleucine, lysine, phenylalanine and valine) were obtained (Baugreet et al, 2019). Cooked restructured steaks made with pea protein (10%) reduced cooking loss indicating that this ingredient could be useful to retain moisture in the product during cooking owing to its high water holding capacity .…”

Antioxidant Peptides from the Protein Hydrolysate of Monkfish (Lophius litulon) Muscle: Purification, Identification, and Cytoprotective Function on HepG2 Cells Damage by H2O2

“…In vitro GI digestion model is widely applied to investigate the digestibility, release of food components, and structural changes under simulated GI conditions [28]. Moreover, the model is popularly used to produce protein hydrolysates because of their safe and efficient properties [11,29]. As shown in Table 1, defatted monkfish muscles were hydrolyzed under in vitro GI digestion, and the degree of hydrolysis (DH, %) of the resulting hydrolysate (referred to as MPTH) was 27.24% ± 1.57%, which was significantly higher than those of hydrolysates using pepsin (23.51 ± 1.96%) and trypsin (20.17% ± 1.55%), individually.…”